Q96JK9 · MAML3_HUMAN
- ProteinMastermind-like protein 3
- GeneMAML3
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1138 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Acts as a transcriptional coactivator for NOTCH proteins. Has been shown to amplify NOTCH-induced transcription of HES1.
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | nuclear speck | |
Cellular Component | nucleoplasm | |
Cellular Component | nucleus | |
Molecular Function | transcription coactivator activity | |
Biological Process | Notch signaling pathway | |
Biological Process | positive regulation of transcription by RNA polymerase II | |
Biological Process | positive regulation of transcription of Notch receptor target |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameMastermind-like protein 3
- Short namesMam-3
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ96JK9
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Nuclear, in a punctate manner.
Keywords
- Cellular component
Disease & Variants
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_046650 | 768 | ||||
Sequence: Missing |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 1,250 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for chain, modified residue (large scale data), modified residue.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000129496 | 1-1138 | UniProt | Mastermind-like protein 3 | |||
Sequence: MGDFAAPAAAANGSSICINSSLNSSLGGAGIGVNNTPNSTPAAPSSNHPAAGGCGGSGGPGGGSAAVPKHSTVVERLRQRIEGCRRHHVNCENRYQQAQVEQLELERRDTVSLYQRTLEQRAKKSGAGTGKQQHPSKPQQDAEAASAEQRNHTLIMLQETVKRKLEGARSPLNGDQQNGACDGNFSPTSKRIRKDISAGMEAINNLPSNMPLPSASPLHQLDLKPSLPLQNSGTHTPGLLEDLSKNGRLPEIKLPVNGCSDLEDSFTILQSKDLKQEPLDDPTCIDTSETSLSNQNKLFSDINLNDQEWQELIDELANTVPEDDIQDLFNEDFEEKKEPEFSQPATETPLSQESASVKSDPSHSPFAHVSMGSPQARPSSSGPPFSTVSTATSLPSVASTPAAPNPASSPANCAVQSPQTPNQAHTPGQAPPRPGNGYLLNPAAVTVAGSASGPVAVPSSDMSPAEQLKQMAAQQQQRAKLMQQKQQQQQQQQQQQQQQQQQQQQQQQQQHSNQTSNWSPLGPPSSPYGAAFTAEKPNSPMMYPQAFNNQNPIVPPMANNLQKTTMNNYLPQNHMNMINQQPNNLGTNSLNKQHNILTYGNTKPLTHFNADLSQRMTPPVANPNKNPLMPYIQQQQQQQQQQQQQQQQQQPPPPQLQAPRAHLSEDQKRLLLMKQKGVMNQPMAYAALPSHGQEQHPVGLPRTTGPMQSSVPPGSGGMVSGASPAGPGFLGSQPQAAIMKQMLIDQRAQLIEQQKQQFLREQRQQQQQQQQQILAEQQLQQSHLPRQHLQPQRNPYPVQQVNQFQGSPQDIAAVRSQAALQSMRTSRLMAQNAGMMGIGPSQNPGTMATAAAQSEMGLAPYSTTPTSQPGMYNMSTGMTQMLQHPNQSGMSITHNQAQGPRQPASGQGVGMVSGFGQSMLVNSAITQQHPQMKGPVGQALPRPQAPPRLQSLMGTVQQGAQSWQQRSLQGMPGRTSGELGPFNNGASYPLQAGQPRLTKQHFPQGLSQSVVDANTGTVRTLNPAAMGRQMMPSLPGQQGTSQARPMVMSGLSQGVPGMPAFSQPPAQQQIPSGSFAPSSQSQAYERNAPQDVSYNYSGDGAGGSFPGLPDGADLVDSIIKGGPGDEWMQELDELFGNP | |||||||
Modified residue (large scale data) | 170 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 351 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 362 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 364 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 370 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 373 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 603 | UniProt | N6-acetyllysine | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 617 | PRIDE | Phosphothreonine | ||||
Sequence: T |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Interaction
Subunit
Interacts through its N-terminal region with the ankyrin repeat region of the Notch proteins NOTCH1, NOTCH2, NOTCH3 and NOTCH4. Forms a DNA-binding complex with Notch proteins and RBPSUH/RBP-J kappa.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q96JK9 | NOTCH1 PRO_0000007676 P46531 | 2 | EBI-1043855, EBI-9692333 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 37-68 | Disordered | ||||
Sequence: PNSTPAAPSSNHPAAGGCGGSGGPGGGSAAVP | ||||||
Region | 119-148 | Disordered | ||||
Sequence: EQRAKKSGAGTGKQQHPSKPQQDAEAASAE | ||||||
Compositional bias | 126-148 | Polar residues | ||||
Sequence: GAGTGKQQHPSKPQQDAEAASAE | ||||||
Region | 169-188 | Disordered | ||||
Sequence: RSPLNGDQQNGACDGNFSPT | ||||||
Compositional bias | 171-185 | Polar residues | ||||
Sequence: PLNGDQQNGACDGNF | ||||||
Region | 207-237 | Disordered | ||||
Sequence: PSNMPLPSASPLHQLDLKPSLPLQNSGTHTP | ||||||
Region | 334-480 | Disordered | ||||
Sequence: EEKKEPEFSQPATETPLSQESASVKSDPSHSPFAHVSMGSPQARPSSSGPPFSTVSTATSLPSVASTPAAPNPASSPANCAVQSPQTPNQAHTPGQAPPRPGNGYLLNPAAVTVAGSASGPVAVPSSDMSPAEQLKQMAAQQQQRAK | ||||||
Compositional bias | 344-426 | Polar residues | ||||
Sequence: PATETPLSQESASVKSDPSHSPFAHVSMGSPQARPSSSGPPFSTVSTATSLPSVASTPAAPNPASSPANCAVQSPQTPNQAHT | ||||||
Compositional bias | 463-480 | Polar residues | ||||
Sequence: SPAEQLKQMAAQQQQRAK | ||||||
Compositional bias | 503-523 | Polar residues | ||||
Sequence: QQQQQQQQHSNQTSNWSPLGP | ||||||
Region | 503-547 | Disordered | ||||
Sequence: QQQQQQQQHSNQTSNWSPLGPPSSPYGAAFTAEKPNSPMMYPQAF | ||||||
Compositional bias | 615-651 | Polar residues | ||||
Sequence: RMTPPVANPNKNPLMPYIQQQQQQQQQQQQQQQQQQP | ||||||
Region | 615-662 | Disordered | ||||
Sequence: RMTPPVANPNKNPLMPYIQQQQQQQQQQQQQQQQQQPPPPQLQAPRAH | ||||||
Region | 691-721 | Disordered | ||||
Sequence: HGQEQHPVGLPRTTGPMQSSVPPGSGGMVSG | ||||||
Compositional bias | 702-716 | Polar residues | ||||
Sequence: RTTGPMQSSVPPGSG | ||||||
Region | 968-991 | Disordered | ||||
Sequence: LQGMPGRTSGELGPFNNGASYPLQ | ||||||
Region | 1024-1084 | Disordered | ||||
Sequence: AAMGRQMMPSLPGQQGTSQARPMVMSGLSQGVPGMPAFSQPPAQQQIPSGSFAPSSQSQAY | ||||||
Compositional bias | 1033-1048 | Polar residues | ||||
Sequence: SLPGQQGTSQARPMVM | ||||||
Compositional bias | 1062-1084 | Polar residues | ||||
Sequence: SQPPAQQQIPSGSFAPSSQSQAY | ||||||
Region | 1090-1109 | Disordered | ||||
Sequence: QDVSYNYSGDGAGGSFPGLP |
Domain
The C-terminal domain is required for transcriptional activation.
Sequence similarities
Belongs to the mastermind family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,138
- Mass (Da)122,293
- Last updated2014-09-03 v4
- Checksum145C1CA5F2F7EEB0
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
H0Y920 | H0Y920_HUMAN | MAML3 | 186 |
Sequence caution
Features
Showing features for compositional bias, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 126-148 | Polar residues | ||||
Sequence: GAGTGKQQHPSKPQQDAEAASAE | ||||||
Compositional bias | 171-185 | Polar residues | ||||
Sequence: PLNGDQQNGACDGNF | ||||||
Compositional bias | 344-426 | Polar residues | ||||
Sequence: PATETPLSQESASVKSDPSHSPFAHVSMGSPQARPSSSGPPFSTVSTATSLPSVASTPAAPNPASSPANCAVQSPQTPNQAHT | ||||||
Compositional bias | 463-480 | Polar residues | ||||
Sequence: SPAEQLKQMAAQQQQRAK | ||||||
Sequence conflict | 486-489 | in Ref. 1; BAB47445, 2; BAG53919, 4; EAX05107 and 5; AAI37132/AAI37131 | ||||
Sequence: Missing | ||||||
Compositional bias | 503-523 | Polar residues | ||||
Sequence: QQQQQQQQHSNQTSNWSPLGP | ||||||
Compositional bias | 615-651 | Polar residues | ||||
Sequence: RMTPPVANPNKNPLMPYIQQQQQQQQQQQQQQQQQQP | ||||||
Compositional bias | 702-716 | Polar residues | ||||
Sequence: RTTGPMQSSVPPGSG | ||||||
Compositional bias | 1033-1048 | Polar residues | ||||
Sequence: SLPGQQGTSQARPMVM | ||||||
Compositional bias | 1062-1084 | Polar residues | ||||
Sequence: SQPPAQQQIPSGSFAPSSQSQAY | ||||||
Sequence conflict | 1064 | in Ref. 1; BAB47445 and 2; BAG53919 | ||||
Sequence: P → H |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AB058719 EMBL· GenBank· DDBJ | BAB47445.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AK123604 EMBL· GenBank· DDBJ | BAG53919.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AC097464 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC104798 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC108053 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC131182 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH471056 EMBL· GenBank· DDBJ | EAX05107.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC137130 EMBL· GenBank· DDBJ | AAI37131.1 EMBL· GenBank· DDBJ | mRNA | ||
BC137131 EMBL· GenBank· DDBJ | AAI37132.1 EMBL· GenBank· DDBJ | mRNA |